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Entry: A0A0S1SBB6_9FLAO
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ID   A0A0S1SBB6_9FLAO        Unreviewed;       377 AA.
AC   A0A0S1SBB6;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   RecName: Full=Histidine biosynthesis bifunctional protein HisB {ECO:0000256|HAMAP-Rule:MF_01022};
DE   Includes:
DE     RecName: Full=Histidinol-phosphatase {ECO:0000256|HAMAP-Rule:MF_01022};
DE              EC=3.1.3.15 {ECO:0000256|HAMAP-Rule:MF_01022};
DE   Includes:
DE     RecName: Full=Imidazoleglycerol-phosphate dehydratase {ECO:0000256|HAMAP-Rule:MF_01022};
DE              Short=IGPD {ECO:0000256|HAMAP-Rule:MF_01022};
DE              EC=4.2.1.19 {ECO:0000256|HAMAP-Rule:MF_01022};
GN   Name=hisB {ECO:0000256|HAMAP-Rule:MF_01022};
GN   ORFNames=SB49_04450 {ECO:0000313|EMBL:ALM07131.1};
OS   Sediminicola sp. YIK13.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Sediminicola.
OX   NCBI_TaxID=1453352 {ECO:0000313|EMBL:ALM07131.1, ECO:0000313|Proteomes:UP000063759};
RN   [1] {ECO:0000313|Proteomes:UP000063759}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YIK13 {ECO:0000313|Proteomes:UP000063759};
RA   Kwon Y.M., Kim S.-J.;
RT   "Genome sequence of Sediminicola sp. YIK13.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ALM07131.1, ECO:0000313|Proteomes:UP000063759}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YIK13 {ECO:0000313|EMBL:ALM07131.1,
RC   ECO:0000313|Proteomes:UP000063759};
RX   PubMed=26823585;
RA   Kwon Y.M., Kim S.J.;
RT   "Complete Genome Sequence of the Proteorhodopsin-Containing Marine
RT   Bacterium Sediminicola sp. YIK13.";
RL   Genome Announc. 4:e01635-15(2016).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-erythro-1-(imidazol-4-yl)glycerol 3-phosphate = 3-(imidazol-
CC         4-yl)-2-oxopropyl phosphate + H2O; Xref=Rhea:RHEA:11040,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:57766, ChEBI:CHEBI:58278; EC=4.2.1.19;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01022};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-histidinol phosphate = L-histidinol + phosphate;
CC         Xref=Rhea:RHEA:14465, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57699, ChEBI:CHEBI:57980; EC=3.1.3.15;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01022};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01022};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC       from 5-phospho-alpha-D-ribose 1-diphosphate: step 6/9.
CC       {ECO:0000256|ARBA:ARBA00005047, ECO:0000256|HAMAP-Rule:MF_01022}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC       from 5-phospho-alpha-D-ribose 1-diphosphate: step 8/9.
CC       {ECO:0000256|HAMAP-Rule:MF_01022}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01022}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the
CC       imidazoleglycerol-phosphate dehydratase family. {ECO:0000256|HAMAP-
CC       Rule:MF_01022}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the histidinol-
CC       phosphatase family. {ECO:0000256|HAMAP-Rule:MF_01022}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01022}.
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DR   EMBL; CP010535; ALM07131.1; -; Genomic_DNA.
DR   RefSeq; WP_062054236.1; NZ_CP010535.1.
DR   AlphaFoldDB; A0A0S1SBB6; -.
DR   STRING; 1453352.SB49_04450; -.
DR   KEGG; syi:SB49_04450; -.
DR   PATRIC; fig|1453352.4.peg.934; -.
DR   OrthoDB; 9790411at2; -.
DR   UniPathway; UPA00031; UER00011.
DR   Proteomes; UP000063759; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004401; F:histidinol-phosphatase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004424; F:imidazoleglycerol-phosphate dehydratase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd07914; IGPD; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   HAMAP; MF_01022; Bifunc_HisB; 1.
DR   HAMAP; MF_00076; HisB; 1.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR006549; HAD-SF_hydro_IIIA.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR020566; His_synth_bifunc_HisB.
DR   InterPro; IPR005954; HisB_N.
DR   InterPro; IPR006543; Histidinol-phos.
DR   InterPro; IPR038494; IGPD_sf.
DR   InterPro; IPR000807; ImidazoleglycerolP_deHydtase.
DR   InterPro; IPR020565; ImidazoleglycerP_deHydtase_CS.
DR   InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR   NCBIfam; TIGR01662; HAD-SF-IIIA; 1.
DR   NCBIfam; TIGR01261; hisB_Nterm; 1.
DR   NCBIfam; TIGR01656; Histidinol-ppas; 1.
DR   PANTHER; PTHR23133:SF2; IMIDAZOLEGLYCEROL-PHOSPHATE DEHYDRATASE; 1.
DR   PANTHER; PTHR23133; IMIDAZOLEGLYCEROL-PHOSPHATE DEHYDRATASE HIS7; 1.
DR   Pfam; PF13242; Hydrolase_like; 1.
DR   Pfam; PF00475; IGPD; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 2.
DR   PROSITE; PS00954; IGP_DEHYDRATASE_1; 1.
DR   PROSITE; PS00955; IGP_DEHYDRATASE_2; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW   Rule:MF_01022};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01022};
KW   Histidine biosynthesis {ECO:0000256|ARBA:ARBA00023102, ECO:0000256|HAMAP-
KW   Rule:MF_01022};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01022, ECO:0000313|EMBL:ALM07131.1};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01022};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01022};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01022};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268, ECO:0000256|HAMAP-
KW   Rule:MF_01022}; Reference proteome {ECO:0000313|Proteomes:UP000063759}.
FT   REGION          1..186
FT                   /note="Histidinol-phosphatase"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01022"
FT   REGION          187..377
FT                   /note="Imidazoleglycerol-phosphate dehydratase"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01022"
FT   ACT_SITE        8
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01022"
FT   ACT_SITE        10
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01022"
FT   BINDING         8
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01022"
FT   BINDING         10
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01022"
FT   BINDING         128
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01022"
SQ   SEQUENCE   377 AA;  43120 MW;  EAC027356E55A558 CRC64;
     MKKVLFIDRD GTIIKETVDE QIDAFDKMIF YPKAFTFLGK IAKELDYELV MITNQDGLGT
     DIFPEDTFWP VHNFILNSFE NEGVVFDKVF LDRTFPHENA PTRKPGTGLL TEYFSDDYDL
     ANSFVIGDRL TDMELAKNLG AKGIFINDNT NLGTGEITVK HEELNDVIAL ENNDWEKIYE
     FLKLKDRVFE INRKTNETDI FIKLNLDGTG KSSIKTGLDF FDHMLDQLAR HGQMDLDIKV
     KGDLEVDEHH TIEDTAIALG EVFHKALGNK LGIERYGFCL PMDDCLAQVA IDFGGRNWLV
     WETEFRREMI GKMPTEMFFH FFKSFTDGAK ANLNIKAEGT NEHHKIEAIF KAFAKAIKMA
     VKRDVEKMVL PSTKGVL
//
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